ID N1P920_YEASC Unreviewed; 580 AA.
AC N1P920;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Cln3p {ECO:0000313|EMBL:EIW12321.1};
GN ORFNames=CENPK1137D_4939 {ECO:0000313|EMBL:EIW12321.1};
OS Saccharomyces cerevisiae (strain CEN.PK113-7D) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=889517 {ECO:0000313|EMBL:EIW12321.1};
RN [1] {ECO:0000313|EMBL:EIW12321.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CEN.PK113-7D {ECO:0000313|EMBL:EIW12321.1};
RA Nijkamp J.F., van den Broek M.A., Datema E., de Kok S., Bosman L.,
RA Luttink M.A., Daran-Lapujade P., Vongsangnak W., Nielsen J., Heijne W.H.M.,
RA Klaassen P., Platt D., Paddon C.J., Koetter P., van Ham R.C.,
RA Reinders M.J.T., Pronk J.T., de Ridder D., Daran J.-M.;
RT "De novo sequencing, assembly and analysis of the genome of the laboratory
RT strain Saccharomyces cerevisiae CEN.PK113-7D, a model for modern industrial
RT biotechnology.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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DR EMBL; CM001522; EIW12321.1; -; Genomic_DNA.
DR AlphaFoldDB; N1P920; -.
DR SMR; N1P920; -.
DR HOGENOM; CLU_033561_1_0_1; -.
DR Proteomes; UP000013192; Chromosome I.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:UniProt.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:UniProt.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:UniProt.
DR CDD; cd20559; CYCLIN_ScCLN_like; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 1.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
DR PANTHER; PTHR10177; CYCLINS; 1.
DR PANTHER; PTHR10177:SF553; G1_S-SPECIFIC CYCLIN CLN3; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; Cyclin-like; 1.
DR PROSITE; PS00292; CYCLINS; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cyclin {ECO:0000256|RuleBase:RU000383}.
FT DOMAIN 113..199
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 454..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 64991 MW; AF6950A7E68DB295 CRC64;
MAILKDTIIR YANARYATAS GTSTATAASV SAASCPNLPL LLQKRRAIAS AKSKNPNLVK
RELQAHHSAI SEYNNDQLDH YFRLSHTERP LYNLTNFNSQ PQVNPKMRFL IFDFIMYCHT
RLNLSTSTLF LTFTILDKYS SRFIIKSYNY QLLSLTALWI SSKFWDSKNR MATLKVLQNL
CCNQYSIKQF TTMEMHLFKS LDWSICQSAT FDSYIDIFLF QSTSPLSPGV VLSAPLEAFI
QQKLALLNNA AGTAINKSSS SQGPSLNINE IKLGAIMLCE LASFNLELSF KYDRSLIALG
AINLIKLSLN YYNSNLWENI NLALEENCQD LDIKLSEISN TLLDIAMDQN SFPSSFKSKY
LNSNKTSLAK SLLDALQNYC IQLKLEEFYR SQELETMYNT IFAQSFDSDS LTCVYSNATT
PKSATVSSAA TDYFSDHTHL RRLTKDSISP PFAFTPTSSS SSPSPFNSPY KTSSSMTTPD
SASHHSHSGS FSSTQNSFKR SLSIPQNSSI FWPSPLTPTT PSLMSNRKLL QNLSVRSKRL
FPVRPMATAH PCSAPTQLKK RSTSSVDCDF NDSSNLKKTR
//
